U.S. patent number 5,445,651 [Application Number 08/256,595] was granted by the patent office on 1995-08-29 for detergent compositions inhibiting dye transfer in washing.
This patent grant is currently assigned to The Procter & Gamble Company. Invention is credited to Adbennaceur Fredj, James P. Johnston, Christiaan A. J. K. Thoen.
United States Patent |
5,445,651 |
Thoen , et al. |
August 29, 1995 |
Detergent compositions inhibiting dye transfer in washing
Abstract
Dye transfer inhibiting compositions are disclosed, comprising:
(A) a metallo catalyst selected from (a) metallo porphin and
water-soluble or water-dispersible derivatives thereof; (b) metallo
porphyrin and water-soluble or water-dispersible derviatives
thereof; (c) metallo phthalocyanine and water-soluble or
water-dispersible derivatives thereof; (B) an enzyme oxidation
scavenger, (C) an enzymatic system capable of generating hydrogen
peroxide, and (D) an enzyme, preferably selected from protease,
lipase, amylase, and cellulase. The enzyme oxidation scavenger (B)
operates to stabilize and protect the enzymes (D) from loss of
activity in the wash.
Inventors: |
Thoen; Christiaan A. J. K.
(Hassdonk, BE), Fredj; Adbennaceur (Brussels,
BE), Johnston; James P. (Overijse, BE) |
Assignee: |
The Procter & Gamble
Company (Cincinnati, OH)
|
Family
ID: |
26132601 |
Appl.
No.: |
08/256,595 |
Filed: |
July 18, 1994 |
PCT
Filed: |
January 22, 1993 |
PCT No.: |
PCT/US93/00625 |
371
Date: |
July 18, 1994 |
102(e)
Date: |
July 18, 1994 |
PCT
Pub. No.: |
WO89/09813 |
PCT
Pub. Date: |
October 19, 1989 |
Foreign Application Priority Data
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Jan 31, 1992 [EP] |
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92870018 |
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Current U.S.
Class: |
8/111; 252/1;
510/303; 510/305; 510/306; 510/320; 510/321; 510/494; 510/500;
510/530; 8/137 |
Current CPC
Class: |
C11D
3/0021 (20130101); C11D 3/38654 (20130101); C11D
3/3932 (20130101) |
Current International
Class: |
C11D
3/38 (20060101); C11D 3/386 (20060101); C11D
3/00 (20060101); C11D 3/39 (20060101); C11D
003/28 (); C11D 003/30 (); C11D 003/386 (); C11D
003/395 () |
Field of
Search: |
;8/111,137
;252/1,102,104,174,174.12,174.17,524,525,542,544,548,529,95 |
References Cited
[Referenced By]
U.S. Patent Documents
Foreign Patent Documents
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0080223 |
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Nov 1982 |
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GB |
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0369678 |
|
Nov 1989 |
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GB |
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0384503 |
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Jan 1990 |
|
GB |
|
89/09813 |
|
Oct 1989 |
|
WO |
|
WO91/0583 |
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May 1991 |
|
WO |
|
Primary Examiner: Albrecht; Dennis
Attorney, Agent or Firm: Jones; Michael D. Yetter; Jerry J.
Rasser; Jacobus C.
Claims
We claim:
1. A dye transfer inhibiting composition comprising:
A. a metallo catalyst present in an amount to provide from about
10.sup.-8 molar to 10.sup.-3 molar in a wash liquor, said metallo
catalyst selected from
a) metallo porphin and water-soluble or water-dispersible
derivatives thereof;
b) metallo porphyrin and water-soluble or water-dispersible
derivatives thereof;
c) metallo phthalocyanine and water-soluble or water-dispersible
derivatives thereof;
B. from about 0.0005 to about 10%, by weight of total composition,
of an enzyme oxidation scavenger, wherein said enzyme oxidation
scavenger is more readily oxidized than enzyme (D) but less readily
oxidized than a dye present is said wash liquor, said enzyme
oxidation scavenger is selected from the group consisting of
i) amines having the formula ##STR9## wherein R.sub.1, R.sub.2,
R.sub.3 are either C.sub.1 -C.sub.1 8 alkoxy groups, aryl groups,
alkyl alcohols or aromatic compounds or where R.sub.1, R.sub.2,
R.sub.3 can be part of an aliphatic or aromatic rings structure
containing nitrogen; and
ii) polyamines having the formula ##STR10## wherein R'.sub.1,
R'.sub.2 are either alkyl groups, aryl groups, alkoxy or alcohols,
n<1 and X is alkyl, alkoxy, aryl,
C. an enzymatic system capable of generating hydrogen peroxide at a
concentration of from 0.005 to 10 ppm/min in said wash liquor;
and
D. a cleaning effective amount of an enzyme selected from the group
consisting of protease lipase, amylase, cellulase, and mixtures
thereof; provided that the residual activity of said enzyme (D) in
the presence of said enzyme oxidation scavenger (C) is at least
60%.
2. A dye transfer inhibiting compositions according to claim 1
wherein said amine base catalyst stabilizer is selected from
imidazole and derivates thereof.
3. A dye transfer inhibiting composition according to claim 1
wherein
4. A dye transfer inhibiting composition according to claim 1
wherein
5. dye transfer inhibiting composition according to claim 1 wherein
said enzymatic system comprises an oxidase and as a substrate an
alcohol, an aldehyde or a combination of both.
6. A dye transfer inhibiting composition according to claim 1,
containing a metallo porphin derivative, wherein said iron porphin
is substituted on at least one of its meso positions with a phenyl
or pyridyl substituent selected from the group consisting of
##STR11## wherein n and m may be 0 or 1, A is selected from the
group consisting of sulfate, sulfonate, phosphate, and carboxylate
groups, and B is selected from the group consisting of C.sub.1
-C.sub.10 alkyl, C.sub.1 -C.sub.10 polyethoxyalkyl and C.sub.1
-C.sub.10 hydroxyalkyl.
7. A dye transfer inhibiting composition according to claim 1
wherein the substituents on the phenyl or pyridyl groups are
selected from the group consisting of --CH.sub.3, --C.sub.2
H.sub.5, --CH.sub.2 CH.sub.2 CH.sub.2 SO.sub.3 --, --CH.sub.2
COO--, --CH.sub.2 C--H(OH)CH.sub.2 SO.sub.3 --, and --SO.sub.3.
8. A dye transfer inhibiting composition according to claims 1,
containing a metallo porphin derivative, wherein said metallo
porphin is substituted on at least one of its meso positions with a
phenyl substituent selected from the group consisting of ##STR12##
wherein X.sup.1 is (=CY-) wherein each Y, independently, is
hydrogen, chlorine, bromine or meso substituted alkyl, cycloalkyl,
aralkyl, aryl, alkaryl or heteroaryl.
9. A dye transfer inhibiting composition according to claim 5
wherein the catalyst compound is metallo tetrasulfonated
tetraphenylporphin.
10. A dye transfer inhibiting composition according to claim 1
wherein the metallo of said metallo catalyst is substituted by Fe,
Mn, Co, Rh, CR, Ru, Mo or other transition metals.
11. A dye transfer inhibiting composition according to claim 1
wherein the concentration of metallo catalyst is from 10.sup.-8 to
10.sup.-3 molar.
12. A dye transfer inhibiting composition according to claim 3
wherein the oxidase is present by 0.1-20000 units per gram of the
composition.
13. A dye transfer inhibiting composition according to claim 3
wherein said substrate is glucose.
14. A dye transfer inhibiting composition according to claim 3
wherein said substrate consists of a C.sub.1 -C.sub.6 alcohol.
15. A dye transfer inhibiting composition according to claim 8
wherein said substrate is ethanol.
16. A dye transfer inhibiting composition according to claim 1 in
which the substrate is present from 0.1 to 50% by weight of the
composition.
17. A dye transfer inhibiting composition according to claims 1
wherein said enzyme oxidation scavenger is present in an amount
from 0.005 to 5% by weight of the total composition.
18. A dye transfer inhibiting composition according to claims 1
which is a detergent additive, in the form of a non-dusting granule
or a liquid.
19. A detergent composition which comprises a dye transfer
inhibiting composition according to claim 1 further comprising an
effective amount of surfactants, builders, and other conventional
detergent ingredients.
20. A process for inhibiting dye transfer between fabrics during
laundering operations involving colored fabrics, said process
comprising contacting said fabrics with a laundering solution
containing a dye transfer inhibition composition according to claim
1.
21. A process for inhibiting dye transfer according to claim 20
which is carried out at a temperature in the range of from
5.degree. C. to 90.degree. C.
22. A process for inhibiting dye transfer according to claim 20
wherein the pH of the bleaching bath is from 7 to 11.
23. A dye transfer inhibiting composition according to claim 11
wherein the concentration of the metallo catalyst is from 10.sup.-6
to 10.sup.-4 molar.
24. A dye transfer inhibiting composition according to claim 12
wherein the oxidase is present at from 0.5 to 5000 units per gram
of the composition.
Description
FIELD OF THE INVENTION
The present invention relates to a composition and a process for
inhibiting dye transfer between fabrics during washing.
BACKGROUND OF THE INVENTION
One of the most persistent and troublesome problems arising during
modern fabric laundering operations is the tendency of some colored
fabrics to release dye into the laundering solutions. The dye is
then transferred onto other fabrics being washed therewith.
One way of overcoming this problem would be to bleach the fugitive
dyes washed out of dyed fabrics before they have the opportunity to
become attached to other articles in the wash.
Suspended or solubilized dyes can to some degree be oxidized in
solution by employing known bleaching agents.
GB 2 101 167 describes a stable liquid bleaching composition
containing a hydrogen peroxide precursor which is activated to
yield hydrogen peroxide on dilution.
However it is important at the same time not to bleach the dyes
actually remaining on the fabrics, that is, not to cause color
damage.
U.S. Pat. No. 4,077,768 describes a process for inhibiting dye
transfer by the use of an oxidizing bleaching agent together with a
catalytic compound such as iron porphins.
Copending EP Patent Application 91202655.6 filed Oct. 9, 1991,
relates to dye transfer inhibiting compositions comprising an
enzymatic system capable of generating hydrogen peroxide and
porphin catalysts.
Due to the presence of the oxidizing agents, the detergent enzymes
such as protease, lipase, amylase, cellulase formulated with said
dye transfer inhibiting composition have to perform their enzymatic
activity in an oxidative environment, with a consequent loss of
activity, especially in the absence of any bleeding dye.
It has now been found that improved stability of enzymes formulated
with said enzymatic dye transfer inhibiting composition can be
achieved by additing enzyme oxidation scavengers.
According to one embodiment of this invention an anzymatic dye
transfer inhibiting composition is provided which is fully
compatible with other enzymes and yet exhibits optimum dye transfer
inhibiting benefits.
Accordingly, a dye transfer inhibiting composition is provided
which exhibits optimum dye transfer inhibiting properties.
According to another embodiment, the invention provides an
efficient process for laundering operations involving colored
fabrics.
SUMMARY OF THE INVENTION
The present invention relates to inhibiting dye transfer
compositions comprising:
A. a metallo catalyst selected from
a) metallo porphin and water-soluble or water-dispersable
derivatives thereof;
b) metallo porphyrin and water-soluble or water-dispersable
derivatives thereof;
c) metallo phthalocyanine and water-soluble or water-dispersable
derivatives thereof;
B. an enzyme oxidation scavenger
C. an enzymatic system capable of generating hydrogen peroxide.
According to another embodiment of this invention a process is also
provided for laundering operations involving colored fabrics.
DETAILED DESCRIPTION OF THE INVENTION
The present invention provides a dye transfer inhibiting
composition comprising:
A. a metallo catalyst selected from
a) metallo porphin and water-soluble or water-dispersable
derivatives thereof;
b) metallo porphyrin and water-soluble or water-dispersable
derivatives thereof;
c) metallo phthalocyanine and water-soluble or water-dispersable
derivatives thereof;
B. an enzyme oxidation scavenger.
C. an enzymatic system capable of generating hydrogen peroxide.
The Hydrogen Peroxide Precursor
The oxidizing agent, hydrogen peroxide is generated in situ by
using an enzymatic hydrogen peroxide generation system.
The use of an enzymatic hydrogen peroxide generating system allows
the continuous generation of low levels of hydrogen peroxide and
provides a practical way of controlling a low steady-state level of
hydrogen peroxide. Maximum effectiveness occurs when the component
levels are such that the hydrogen peroxide is replenished at a rate
similar to its removal due to the oxidation of dyes in the wash
water. The enzyme used in the present invention is an oxidase. The
oxidase is present by 0.1-20000 units, preferably 0.5 to 5000 units
per gram of the composition. One unit is the amount of enzyme
needed to convert 1 .mu.mol of substrate per minute.
Suitable oxidases are urate oxidase, galactose oxidase, alcohol
oxidases, amine oxidases, amino acid oxidases, cholesterol oxidase
and glucose oxidase, malate oxidase, glycollate oxidase, hexose
oxidase, aryl alcohol oxidase, L-gulonolactose oxidase, pyranose
oxidase, L-sorbose oxidase, pyridoxine 4-oxidase, 2-2-hydroxyacid
oxidase, choline oxidase, ecdysone oxidase.
The preferred enzymatic systems are alcohol and aldehyde oxidases,
glucose oxidase.
The more preferred systems for granular detergent application would
have solid alcohols, e.g. glucose whose oxidation is catalyzed by
glucose oxidase to glucoronic acid with the formation of hydrogen
peroxide.
The more preferred systems for liquid detergent application would
involve liquid alcohols which could for example, also act as
solvents. An example is ethanol/ethanol oxidase.
The quantity of oxidase to be employed in compositions according to
the invention should be at least sufficient to provide in the wash
a constant generation of 0.005 to 10 ppm AvO per minute. For
example, with the glucose oxidase, this can be achieved at room
temperature and at pH 6 to 11, preferentially 7 to 9 with 1-20000
U/l glucose oxidase, 0.005 to 0.5% glucose under constant aeration
in the washing process.
Metallo Catalyst
The preferred usage range of the catalyst in the wash is 10.sup.-8
molar to 10.sup.-3 molar, more preferred 10.sup.-6 -10.sup.-4
molar.
The essential metallo porphin structure may be visualized as
indicated in Formula I in the accompanying drawings. In Formula I
the atom positions of the porphin structure are numbered
conventionally and the double bonds are put in conventionally. In
other formula, the double bonds have been omitted in the drawings,
but are actually present as in I.
Preferred metallo porphin structures are those substituted at one
or more of the 5, 10, 15 and 20 carbon positions of Formula I (Meso
positions), with a phenyl or pyridyl substituent selected from the
group consisting of ##STR1## wherein n and m may be 0 or 1; A may
be sulfate, sulfonate, phosphate or carboxylate groups; and B is
C.sub.1 -C.sub.10 alkyl, polyethoxy alkyl or hydroxy alkyl.
Preferred molecules are those in which the substituents on the
phenyl or pyridyl groups are selected from the group consisting of
--CH.sub.3, --C.sub.2 H.sub.5, --CH.sub.2 CH.sub.2 CH.sub.2
SO.sub.3 --, --CH.sub.2 --, and --CH.sub.2 CH(OH)CH.sub.2 SO.sub.3
--, --SO.sub.3.
A particularly preferred metallo phorphin is one in which the
molecule is substituted at the 5, 10 15, and 20 carbon positions
with the substituent ##STR2##
This preferred compound is known as metallo tetrasulfonated
tetraphenylporphin. The symbol X.sup.1 is (.dbd.CY--) wherein each
Y, independently, is hydrogen, chlorine, bromine or meso
substituted alkyl, cycloalkyl, aralkyl, aryl, alkaryl or
heteroaryl.
The symbol X.sup.2 of Formula I represents an anion, preferably
OH.sup.-- or Cl.sup.--. The compound of Formula I may be
substituted at one or more of the remaining carbon positions with
C.sub.1 -C.sub.10 alkyl, hydroxyalkyl or oxyalkyl groups.
##STR3##
Porphin derivatives also include chlorophylls, chlorines, i.e.
isobacterio chlorines and bacteriochlorines.
Metallo porphyrin and water-soluble or water-dispersable
derivatives thereof have a structure given in formula II. ##STR4##
where X can be alkyl, alkyl carboxy, alkyl hydroxyl, vinyl,
alkenyl, alkyl sulfate, alkylsulfonate, sulfate, sulfonate,
aryl.
The symbol X.sup.2 of Formula II represents an anion, preferably
OH.sup.-- or Cl.sup.--.
The symbol X.sub.i can be alkyl, alkylcarboxy, alkylhydroxyl,
vinyl, alkenyl, alkylsulfate, alkylsulfonate, sulfate,
sulfonate.
Metallo phthalocyanine and derivatives have the structure indicated
in Formula III, wherein the atom positions of the phthalocyanine
structure are numbered conventionally. The anionic groups in the
above structures contain cations selected from the group consisting
of sodium and potassium cations or other non-interfering cations
which leave the structures water-soluble. Preferred phthalocyanine
derivatives are metallo phthalocyanine trisulfonate and metallo
phthalocyanine tetrasulfonate. ##STR5##
Another form of substitution possible for the present invention is
substitution of the central metal by Fe, Mn, Co, Rh, Cr, Ru, Mo or
other transition metals.
Still a number of considerations are significant in selecting
variants of or substituents in the basic porphin or azaporphin
structure. In the first place, one would choose compounds which are
available or can be readily synthesized.
Beyond this, the choice of the substituent groups can be used to
control the solubility of the catalyst in water or in detergent
solutions. Yet again, especially where it is desired to avoid
attacking dyes attached to solid surfaces, the substituents can
control the affinity of the catalyst compound for the surface.
Thus, strongly negatively charged substituted compounds, for
instance the tetrasulfonated porphin, may be repelled by negatively
charged stains or stained surfaces and are therefore most likely
not to cause attack on fixed dyes, whereas the cationic or
zwitterionic compounds may be attracted to, or at least not
repelled by such stained surfaces.
Enzyme Oxidation Scavenger
According to the present invention, it has now been found that
improved stability of enzymes formulated with enzymatic dye
transfer inhibiting compositions can be achieved by adding enzyme
oxidation scavengers.
By enzyme oxidation scavengers is meant any chemical compound
which, in the presence of the enzymatic dye transfer inhibiting
system, is more readily oxidized than the enzyme but which is less
readily oxidized than the dye bleeding from the fabrics. The enzyme
oxidation scavengers of the present invention meet the following
criteria:
First, the residual activity of the enzyme in the presence of the
enzyme oxidation scavenger formulated with the dye transfer
inhibiting composition of the present invention should be at least
60%, preferably more than 75% after 10 minutes of stirring at
20.degree. C.
The amount of enzyme oxidation scavenger to be used in the present
invention is dependent on the specific scavenger chosen and should
be such that the above criteria has been met.
Thus, according to the present invention, a dye transfer inhibiting
composition is provided which inhibits dye transfer while not
adversely affecting the activity of the enzymes formulated
therewith.
Preferred enzyme oxidation scavengers suitable for the present
invention are amines and preferably tertiary amines having the
formula ##STR6## wherein R.sub.i, R.sub.1 and R.sub.2 are either
C.sub.1 -C.sub.18 alkyl groups, aryl groups, alkyl alcohols or
aromatic compounds; or wherein R.sub.i, R.sub.1 and R.sub.2 can be
part of an aliphatic or aromatic ring structure containing
nitrogen.
Most preferred tertiary amines are compounds having the formula I
wherein R.sub.1 =R.sub.2 =C.sub.2 H.sub.5, R.sub.3 =C.sub.2 H.sub.4
OH
Other amines suitable for use as enzyme oxidation scavengers in the
present invention are alkoxylated polyamines. Such materials can be
conveniently represented as molecules of the empirical structures
with repeating units: ##STR7## where R'.sub.1, R'.sub.2 are either
C.sub.1 -C.sub.18 alkyl groups, aryl groups, alkoxy or
alkylalcohols, n>1 and X is an alkyl, aryl, substituted alkyl or
aryl, alkoxy.
Most preferred are polyamines wherein R'.sub.1 =R'.sub.2 =CH.sub.2,
X=(CH.sub.2 CH.sub.2 O).sub.m OH, 1<n<12 and
5<m<20.
The level of the enzyme oxidation scavenger in the detergent
composition is preferably from 0.0005 to 10%, more preferred from
0.001 to 7%, most preferred from 0.005 to 5%.
The present compositions are conveniently used as additives to
detergent compositions for the main wash cycle.
The present invention also encompasses dye transfer inhibiting
compositions which will comprise detergent ingredients and thus
serve as detergent compositions.
The enzymes that can be formulated with present compositions are
enzymes which can be active in the removal of soils or stains such
as protease, lipase, amylase, carboxylase, peroxidases, cellulase
or mixtures thereof.
DETERGENT INGREDIENTS
A wide range of surfactants can be used in the detergent
compositions. A typical listing of anionic, nonionic, ampholytic
and zwitterionic classes, and species of these surfactants, is
given in U.S. Pat. No. 3,644,961 issued to Norris on May 23,
1972.
Mixtures of anionic surfactants are particularly suitable herein,
especially mixtures of sulphonate and sulphate surfactants in a
weight ratio of from 5:1 to 1:2, preferably from 3:1 to 2:3, more
preferably from 3:1 to 1:1. Preferred sulphonates include alkyl
benzene sulphonates having from 9 to 15, especially 11 to 13 carbon
atoms in the alkyl radical, and alpha-sulphonated methyl fatty acid
esters in which the fatty acid is derived from a C.sub.12 -C.sub.18
fatty source preferably from a C.sub.16 -C.sub.18 fatty source. In
each instance the cation is an alkali metal, preferably sodium.
Preferred sulphate surfactants are alkyl sulphates having from 12
to 18 carbon atoms in the alkyl radical, optionally in admixture
with ethoxy sulphates having from 10 to 20, preferably 10 to 16
carbon atoms in the alkyl radical and an average degree of
ethoxylation of 1 to 6. Examples of preferred alkyl sulphates
herein are tallow alkyl sulphate, coconut alkyl sulphate, and
C.sub.14-15 alkyl sulphates. The cation in each instance is again
an alkali metal cation, preferably sodium.
One class of nonionic surfactants useful in the present invention
are condensates of ethylene oxide with a hydrophobic moiety to
provide a surfactant having an average hydrophilic-lipophilic
balance (HLB) in the range from 8 to 17, preferably from 9.5 to
13.5, more preferably from 10 to 12.5. The hydrophobic (lipophilic)
moiety may be aliphatic or aromatic in nature and the length of the
polyoxyethylene group which is condensed with any particular
hydrophobic group can be readily adjusted to yield a water-soluble
compound having the desired degree of balance between hydrophilic
and hydrophobic elements.
Especially preferred nonionic surfactants of this type are the
C.sub.9 -C.sub.15 primary alcohol ethoxylates containing 3-8 moles
of ethylene oxide per mole of alcohol, particularly the C.sub.14
-C.sub.15 primary alcohols containing 6-8 moles of ethylene oxide
per mole of alcohol and the C.sub.12 -C.sub.14 primary alcohols
containing 3-5 moles of ethylene oxide per mole of alcohol.
Another class of nonionic surfactants comprises alkyl polyglucoside
compounds of general formula
wherein Z is a moiety derived from glucose; R is a saturated
hydrophobic alkyl group that contains from 12 to 18 carbon atoms; t
is from 0 to 10 and n is 2 or 3; x is from 1.3 to 4, the compounds
including less than 10% unreacted fatty alcohol and less than 50%
short chain alkyl polyglucosides. Compounds of this type and their
use in detergent are disclosed in EP-B 0 070 077, 0 075 996 and 0
094 118.
Also suitable as nonionic surfactants are polyhydroxy fatty acid
amide surfactants of the formula ##STR8## wherein R.sup.1 is H, or
R.sup.1 is C.sub.1-4 hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl
or a mixture thereof, R.sup.2 is C.sub.5-31 hydrocarbyl, and Z is a
polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at
least 3 hydroxyls directly connected to the chain, or an
alkoxylated derivative thereof. Preferably, R.sup.1 is methyl,
R.sup.2 is a straight C.sub.11-15 alkyl or alkenyl chain such as
coconut alkyl or mixtures thereof, and Z is derived from a reducing
sugar such as glucose, fructose, maltose, lactose, in a reductive
amination reaction.
The compositions according to the present invention may further
comprise a builder system. Any conventional builder system is
suitable for use herein including aluminosilicate materials,
silicates, polycarboxylates and fatty acids, materials such as
ethylenediamine tetraacetate, metal ion sequestrants such as
aminopolyphosphonates, particularly ethylenediamine tetramethylene
phosphonic acid and diethylene triamine pentamethylenephosphonic
acid. Though less preferred for obvious environmental reasons,
phosphate builders can also be used herein.
Suitable builders can be an inorganic ion exchange material,
commonly an inorganic hydrated aluminosilicate material, more
particularly a hydrated synthetic zeolite such as hydrated zeolite
A, X, B or HS.
Another suitable inorganic builder material is layered silicate,
e.g. SKS-6 (Hoechst). SKS-6 is a crystalline layered silicate
consisting of sodium silicate (Na.sub.2 Si.sub.2 O.sub.5).
Suitable polycarboxylates builders for use herein include citric
acid, preferably in the form of a water-soluble salt, derivatives
of succinic acid of the formula R-CH(COOH)CH2(COOH) wherein R is
C10-20 alkyl or alkenyl, preferably C12-16, or wherein R can be
substituted with hydroxyl, sulfo sulfoxyl or sulfone substituents.
Specific examples include lauryl succinate, myristyl succinate,
palmityl succinate 2-dodecenylsuccinate, 2-tetradecenyl succinate.
Succinate builders are preferably used in the form of their
water-soluble salts, including sodium, potassium, ammonium and
alkanolammonium salts.
Other suitable polycarboxylates are oxodisuccinates and mixtures of
tartrate monosuccinic and tartrate disuccinic acid such as
described in U.S. Pat. No. 4,663,071.
Especially for the liquid execution herein, suitable fatty acid
builders for use herein are saturated or unsaturated C10-18 fatty
acids, as well as the corresponding soaps. Preferred saturated
species have from 12 to 16 carbon atoms in the alkyl chain. The
preferred unsaturated fatty acid is oleic acid. Another preferred
builder system for liquid compositions is based on dodecenyl
succinic acid.
Preferred builder systems for use in granular compositions include
a mixture of a water-insoluble aluminosilicate builder such as
zeolite A, and a watersoluble carboxylate chelating agent such as
citric acid.
Other builder materials that can form part of the builder system
for use in granular compositions for the purposes of this invention
include inorganic materials such as alkali metal carbonates,
bicarbonates, silicates, and organic materials such as the organic
phosphonates, amino polyalkylene phosphonates and amino
polycarboxylates.
Other suitable water-soluble organic salts are the homo- or
co-polymeric acids or their salts, in which the polycarboxylic acid
comprises at least two carboxyl radicals separated from each other
by not more than two carbon atoms.
Polymers of this type are disclosed in GB-A-1,596,756. Examples of
such salts are polyacrylates of MW 2000-5000 and their copolymers
with maleic anhydride, such copolymers having a molecular weight of
from 20,000 to 70,000, especially about 40,000.
Detergency builder salts are normally included in amounts of from
10% to 80% by weight of the composition preferably from 20% to 70%
and most usually from 30% to 60% by weight.
The compositions of the present invention should be free from
conventional bleaching agents. Other components used in detergent
compositions may be employed, such as suds boosting or depressing
agents, enzymes and stabilizers or activators therefore,
soil-suspending agents soil-release agents, optical brighteners,
abrasives, bactericides, tarnish inhibitors, coloring agents, and
perfumes. Especially preferred are combinations with enzyme
technologies which also provide a type of color care benefit.
Examples are cellulase for color maintenance/rejuvenation.
These components, particularly the enzymes, optical brighteners,
coloring agents, and perfumes, should preferably be chosen such
that they are compatible with the bleach component of the
composition.
The detergent compositions according to the invention can be in
liquid, paste or granular forms. Granular compositions according to
the present invention can also be in "compact form", i.e. they may
have a relatively higher density than conventional granular
detergents, i.e. from 550 to 950 g/l; in such case, the granular
detergent compositions according to the present invention will
contain a lower amount of "inorganic filler salt", compared to
conventional granular detergents; typical filler salts are alkaline
earth metal salts of sulphates and chlorides, typically sodium
sulphate; "compact" detergents typically comprise not more than 10%
filler salt.
The present invention also relates to a process for inhibiting dye
transfer from one fabric to another of solubilized and suspended
dyes encountered during fabric laundering operations involving
colored fabrics.
The process comprises contacting fabrics with a laundering solution
as hereinbefore described.
The process of the invention is conveniently carried out in the
course of the washing process. The washing process is preferably
carried out at 5.degree. C. to 90.degree. C., especially 20 to 60,
but the catalysts are effective at up to 95.degree. C. The pH of
the treatment solution is preferably from 7 to 11, especially from
7.5 to 10.5.
The process and compositions of the invention can also be used as
additive during laundry operations.
The following examples are meant to exemplify compositions of the
present invention, but are not necessarily meant to limit or
otherwise define the scope of the invention, said scope being
determined according to claims which follow.
General Test Conditions
To assess the stabilizing effect of the enzyme oxidation scavenger
on the enzyme, the samples need to be free of dye since the dye
also acts as a enzyme oxidation scavenger. The stability of the
enzyme formulated with dye transfer inhibiting compositions are
compared in the absence and presence of the enzyme oxidation
scavenger. More in particular, the stability of protease was
determined in the presence of iron porphin catalyst and glucose
oxidase/glucose system.
I) in absence of enzyme oxidation scavenger
II) in presence of enzyme oxidation scavenger
Protease Activity
The protease activity is determined spectrophotometrically by
measuring the absorbance at a wavelength of 410 nm. This
corresponds to the formation of p-nitroaniline, which is the
product of cleavage by a protease of a
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide. This pNA substrate (i.e.
Succinyl Ala-Ala . . . ) is dissolved in dimethylsulfoxide (DMSO)
using 1 ml or DMSO for 50 mg of the substrate. The dissolved
substrate is kept frozen. Before testing for protease activity, a
solution of the PNA substrate is prepared by diluting the substrate
in Tris-buffer, pH 8.0 using a volume ratio of 1:20.
Approximately 100 .mu.l of the diluted pNA substrate is added to a
1 ml sample, of the solution (I) or (II) to be analyzed, in a
cuvette. The sample is then introduced in the spectrophotometer and
the absorbance at 410 nm is monitored for approximately 5 min. The
absorbance curve should be a straight line over the first few
minutes (ca. 3 min). If this is not the case, then the solution (I)
or (II) should be diulted with Tris-buffer. For instance, using the
protease B Ex Genencor in the concentration mentioned above, the
sample that gives a linear response is 100 .mu.l of the solution
and 900 .mu.l of Tris-buffer, pH 8.0 (i.e. a dilution ratio of
1:9). A sample of the solution containing Savinase.TM. in the
mentioned concentration gives a linear absorbance response (i.e.
does not need to be diluted).
The slope of the absorbance curve is an indication of the protease
activity. The % residual activity of solution (I) and (II) is
determined relative to the slope obtained before adding the iron
porphin catalyst and glucose/osidase system.
Dye Oxidation
The extent of dye oxidation is determined in a 100 mM phosphate
buffer solution of 100 ml. The solution is continuously stirred in
a beaker at a constant rate using a magnetic stirrer. The % of due
oxidized is determined spectrophotometrically.
EXAMPLE 1
A. 0.1M phosphate buffer solution was prepared and its pH adjusted
to 8.0. Then four 100 ml samples were prepared in separate beakers
with the following compositions:
______________________________________ solution A: 0.1 glucose
oxidase units/ml 10 ppm FE(III)TPPS 0.1% glucose 1.1 ppm BPN'
(Ex-Genencor) solution B: solution A + scavenger solution C: 0.1
glucose oxidase units/ml 10 ppm Fe(III)TPPS 0.1% glucose 40 ppm
Direct Blue (CI #24410), absorbance peak at 600 nm solution D:
solution C + scavenger ______________________________________
The solutions were stirred at room temperature using a magnetic
stirrer. The stability of protease and the amount of oxidized dye
were determined according to the methods described in the text.
______________________________________ % residual activity solution
or protease % dye oxidized after 10 mins after 30 min
______________________________________ without scavenger 45 77
0.05% dimethylaminoethanol 75 76 0.01% diethylaminoethanol 83 77
______________________________________
EXAMPLE II
The stability of protease B (Ex-genecor) was studied at a pH of 7.8
using the same concentrations and experimental conditions as
example 1 except that the solution now contains 1% detergent. The
ternary amine that was used for this test was an ethoxylated tetra
ethylene pent amine (MW=4800) in a concentration of 30 ppm.
______________________________________ activity % residual solution
or protease % dye oxidized after 10 mins after 30 min
______________________________________ without scavenger 25 100
with scavenger 100 100 ______________________________________
EXAMPLE III
This experiment is similar to the one described in example I except
for the following details: glucose oxidase concentration: 2
units/ml Fe(III) TPPS concentraion: 5 ppm enzyme: Savinase.RTM.
(Ex-Novo) 32E-6 KNPU/ml 40 ppm Acid Red 151 (CI #26900), absorbance
peak at (480-490 nm) 0.1M phosphate buffer at pH 10.5
______________________________________ activity % residual solution
or protease % dye oxidized after 10 mins after 30 min
______________________________________ without scavenger 16 95
0.05% dimethylaminoethanol 90 95
______________________________________
EXAMPLE IV
A liquid dye transfer inhibiting composition according to the
present invention is prepared, having the following
compositions:
______________________________________ %
______________________________________ Linear alkylbenzene
sulfonate 10 Alkyl sulphate 4 Fatty alcohol (C.sub.12 -C.sub.15)
ethoxylate 12 Fatty acid 10 Oleic acid 4 Citric acid 1 NaOH 3.4
Propanediol 1.5 Ethanol 5 Ethanoloxidase 5 u/ml Ferric
tetrasulfonated tetraphenylporphin 0.1 ethoxylated tatraethylene
pentamine 0.3 protease B ex-Genencor 0.33 Minors up to 100
______________________________________
EXAMPLE V
A compact granular dye transfer inhibiting composition according to
the present invention is prepared, having the following
formulation:
______________________________________ %
______________________________________ Linear alkyl benzene
sulphonate 11.40 Tallow alkyl sulphate 1.80 C.sub.45 alkyl sulphate
3.00 C.sub.45 alcohol 7 times ethoxylated 4.00 Tallow alcohol 11
times ethoxylated 1.80 Dispersant 0.07 Silicone fluid 0.80
Trisodium citrate 14.00 Citric acid 3.00 Zeolite 32.50 Maleic acid
actylic acid copolymer 5.00 DETMPA 1.00 Cellulase (active protein)
0.03 Alkalase/BAN 0.60 Lipase 0.36 Sodium silicate 2.00 Sodium
sulphate 3.50 Ferric tatrasulfonated tetraphenylporphin 0.025
Glucose 10.00 Glucose oxidase 100 u/ml diethylaninoethanol 0.05
Minors up to 100 ______________________________________
* * * * *